1y9a

Alcohol Dehydrogenase from Entamoeba histolotica in complex with cacodylate
(see also Tetrameric alcohol dehydrogenases)



Superposition of the structures of the wild-type apo-EhADH1 (colored lime, 1y9a) and the apo D275P-EhADH1 mutant (colored orange) (2oui). Pro275 and Asp275 are labeled red. Residues within a distance of 4 Å from the mutation are shown (names of monomers are in brackets). Replacing Asp275 with Pro significantly enhanced the thermal stability of EhADH1: ΔT1/260min = +9.3°C, ΔT1/2CD = +10°C. The reverse mutation in the thermophilic TbADH (1ykf; colored magenta ) - substitution of wt TbADH Pro275 with Asp (2nvb; colored cyan ) reduced the thermal stability of the enzyme: ΔT1/260min = -13.8°C, ΔT1/2CD = -18.8°C. Nitrogen and oxygen atoms are colored in CPK colors. Pro275 and Asp275 are labeled red (names of monomers are in brackets). These findings indicate that a single proline mutation is responsible for the significant differences in the thermal stability of ADHs, and show the importance of prolines in the protein stability. It was also shown that substitution by proline at the important positions could significantly stabilize the protein.

About this Structure
1Y9A is a 2 chains structure of sequences from Entamoeba histolytica. Full crystallographic information is available from OCA.

Reference
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